Titlebook: Natriuretic Peptides in Health and Disease; Willis K. Samson,Ellis R. Levin Book 1997 Humana Press Inc. 1997 biochemistry.endothelium.grow

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Ellis R. Levinn problem; query processing techniques and architectures; tools and mashups for application development; the application of search computing to bio-informatics; and the exploitation potentials of project results..978-3-642-19667-6978-3-642-19668-3Series ISSN 0302-9743 Series E-ISSN 1611-3349

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The Guanylyl Cyclase-A Receptor,e (ANP) and probably B-type natriuretic peptide (BNP). This isoform, known as the guanylyl cyclase-A (GC-A; NPR-A) receptor, is similar in overall topology to that of all other known membrane forms of guanylyl cyclases in that it contains an extracellular ligand-binding domain, a single transmembran

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Cellular and Molecular Aspects of the A-Type Natriuretic Peptide,t suggestive evidence that these structures might function as endocrine organs came from the studies of Kisch . that demonstrated the presence of membrane-bound secretory granules within atrial myocytes, a finding that was confirmed in the studies of Jamison and Palade . several years later. In 1981

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Cellular and Molecular Biology of B-Type Natriuretic Peptide,blood pressure. Both ANP and BNP appear to be potent natriuretic and diuretic hormones that are also capable of decreasing the activity of the renin/angiotensin/aldosterone system and also possess vasodilatory activities. In contrast, CNP appears to possess more potent vasodilatory activity and less

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Cellular and Molecular Aspects of C-Type Natriuretic Peptide (CNP),g of 22 amino acids, and the ring portion consisting of 17 amino acids is highly homologous to α-ANP and BNP (Fig. 1). Different from ANP and BNP, CNP lacks the C-terminal tail, and has a Cys residue at the C-terminus. Another species of CNP is CNP-53, which has the N-terminal extension of 31 amino

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